ID   A0A182Q234_9DIPT        Unreviewed;      1143 AA.
AC   A0A182Q234;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
OS   Anopheles farauti.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF001568-PA, ECO:0000313|Proteomes:UP000075886};
RN   [1] {ECO:0000313|Proteomes:UP000075886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AFAF001568-PA}
RP   IDENTIFICATION.
RC   STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF001568-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; AXCN02000243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182Q234; -.
DR   STRING; 69004.A0A182Q234; -.
DR   EnsemblMetazoa; AFAF001568-RA; AFAF001568-PA; AFAF001568.
DR   VEuPathDB; VectorBase:AFAF001568; -.
DR   OrthoDB; 216092at2759; -.
DR   Proteomes; UP000075886; Unassembled WGS sequence.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd07103; ALDH_F5_SSADH_GabD; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          672..1136
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   REGION          403..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        913
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   1143 AA;  126726 MW;  058D3A2C700E7D07 CRC64;
     MKSANRPVPG VAMAGAVSTL GSQVDEMKVK KKSSRKISAP PWLKGRLVGA KAKGDKSVPA
     APCCGVEVAE ERIDRLEERQ FEDKSVQCDD LLPYDGHRFG SHRNSSDRCS SCCHPVNPIY
     QTNLIVNQIP FMDDELDDGA LATFQRNHHA VRQRRNSRID GTPIPSQALF RKNNIFATPN
     GTSDEMRRSL TTLSHNNLQD WNRSHLAQSE VSIPNSIEYD QSVSMASVER SKPRVPLRRK
     AGAYGNVTLN VQIANGMNTT ILEAPDKPVV PRRRYGVAPD RRTICESQRS NQSPSQSSCL
     VLGMNSDARN PLNYKMYTPF YNKRQTMPPE HFKNWPSASR YDDENELHYR TLSYYSEVSN
     QLEQYERRSS FDTGSSRLLN AIDSNSIMYR SSMDNLPKVS ERIAEEEPTP PESGPRFRKP
     HVGKYPATDN GANRLNRNGP NVRAKNMPND RSAAQTQSNL LAPPTTGTFG RWSGSIQNLF
     SIGNRASNGA GRWSKSENCL NEVGQQRQQH QRVAHSQRGS SKPWADRLFG RTGKHGRSRR
     TNTFLTSGGG SFFTYKYDDE EESAWQKYFS LGMLRKIRPK PGKPSRGKDD SRLQRSRSQC
     ESTLAGIKMD EEAMWKGFYD KIQEQKQKAP TEHQSIKWAS GSGVRLSAVI NITRAMHSNP
     LKQSQAFVNG RWVGARSGAT FDVQNPANGQ VLGAVPDMTR DDVQLAIDAA HEAFYEKSWH
     NSTAKERAAL LKNWYALMEK NRQEIASIMT AESGKPLVES LGEVTYGNSF VEWFAEEARR
     IYGEIVPPPV ANRQIMMTRQ PVGVAGLITP WNFPHAMITR KAAAAIAAGC TVVIKPAEDT
     PLTALALARL AEEAGFPKGV INVITSSRTH AAEIGQLLCG SDKVAAISFT GSTEVGKQLY
     RQCADGVKRI GLELGGNAPF IVFKSADMEK ALTGAMNSKF RNCGQTCISA NRFLIQDEVH
     DDFVEKLIGR IGKLAVGDGS REGVQIGPLI NQAQLKKVEQ FVQDAKDKGA TIRCGGRKLP
     NHGPLYYEPT VVTDLRDNML LYNEEVFGPV VSVVRFKTEE EALAIANSTR RGLAGYFFSN
     DLNQVFRVGK LLETGMIGIN EGLISATEAA FGGIKESGIG REGSRHGIDE YVYIKYLCYG
     NLQ
//